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Metalloprotein - Crossref

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Last Updated: 23 April 2022

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Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR

We provide a new platform to enable structural and dynamic determination of large metalloproteins using solid-state nuclear magnetic resonance with 1 H detection under ultrafast magic angle rotation. The device on which we show these methods is based is the enzyme Cu, Zn superoxide dismutase, which coordinates a Cu ion that is available in Cu + or Cu 2+ forms. Timescales for movement are estimated to be within a range of the overall correlation time in solution, where internal movements that are not observable here would not be apparent.

Source link: https://doi.org/10.1073/pnas.1204515109


Allosteric control in a metalloprotein dramatically alters function

We investigated both theoretically and experimentally whether distal regions could influence the metal center in the diabetes drug target MitoNEET. We show that a loop 20 away from the metal center exerts allosteric control over the cluster binding domain and manages multiple properties of the metal center. Mutagenesis of L2 results in dramatic shifts in the redox potential of the [2Fe-2S] cluster and orders of magnitude, as demonstrated by the rate of [2Fe-2S] cluster shift to an apo-acceptor protein. Twisting in L2 controls scissor dynamics in the cluster binding domain, resulting in disruptions of one of the cluster-coordinating histidines, according to an investigation of the native basin dynamics of the protein using all-atom simulations. These allosteric results are in accordance with previous folding simulations that predicted that L2 would communicate with residues around the metal center, according to previous folding experiments.

Source link: https://doi.org/10.1073/pnas.1208286110


X-ray structure analysis of a metalloprotein with enhanced active-site resolution using in situ x-ray absorption near edge structure spectroscopy

The X-ray absorption spectroscopy is highly sensitive to an absorbing atom's coordination, which allows bond distances and angles of the immediate atomic cluster to be determined with atomic precision. We show that the combination of both methods on the same metalloprotein single crystal yields a structural model of the protein with exceptional active-site resolution. We have obtained x-ray diffraction data set to 1. 4-degree resolution and Fe K-edge polarized x-ray absorption near edge structure spectra on the same cyanomet sperm whale myoglobin crystal, which comes to this conclusion. We have obtained a cyanomet sperm whale myoglobin structural model with a greater degree of the bond lengths and angles at the active site than would have been possible with crystallographic analysis alone, thanks to combining XANES and x-ray diffraction.

Source link: https://doi.org/10.1073/pnas.0608411104


X-ray damage to the Mn 4 Ca complex in single crystals of photosystem II: A case study for metalloprotein crystallography

Quantification of damage caused by x-rays exposure to Mn 4 Ca's active site in single crystals of photosystem II was determined by dose and mass, temperature, and time. The x-ray absorption spectra reveal that the structure changes from one that is typical of a high-valent Mn 4 Ca cluster to that of Mn in a squeous solution to that of Mn in a neous solution.

Source link: https://doi.org/10.1073/pnas.0505207102

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

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* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions